Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-02655-1
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Funding
- University of Chicago
- National Institute of General Medical Sciences of the National Institutes of Health [R35 GM119840]
- National Cancer Institute [RO1 CA200310]
- University of Chicago Medicine Comprehensive Cancer Center [P30 CA14599]
- Chicago Biomedical Consortium
- Searle Funds at The Chicago Community Trust
- Research Fellowship from the Alfred P. Sloan Foundation
- EPFL
- Swiss National Science Foundation
- European Research Council under the European Union's Seventh Framework Programme (FP)/ERC Grant [340260-PalmERa']
- Human Frontier Science Program [LT000152/2014-L]
- Swiss SystemsX.ch initiative [TPdF 2013/143]
- NATIONAL CANCER INSTITUTE [R01CA216242, R01CA200310, P30CA014599] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R35GM119840] Funding Source: NIH RePORTER
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The reversible modification of cysteine residues by thioester formation with palmitate (S-palmitoylation) is an abundant lipid post-translational modification (PTM) in mammalian systems. S-palmitoylation has been observed on mitochondrial proteins, providing an intriguing potential connection between metabolic lipids and mitochondrial regulation. However, it is unknown whether and/or how mitochondrial S-palmitoylation is regulated. Here we report the development of mitoDPPs, targeted fluorescent probes that measure the activity levels of erasers of S-palmitoylation, acyl-protein thioesterases (APTs), within mitochondria of live cells. Using mitoDPPs, we discover active S-depalmitoylation in mitochondria, in part mediated by APT1, an S-depalmitoylase previously thought to reside in the cytosol and on the Golgi apparatus. We also find that perturbation of long-chain acyl-CoA cytoplasm and mitochondrial regulatory proteins, respectively, results in selective responses from cytosolic and mitochondrial S-depalmitoylases. Altogether, this work reveals that mitochondrial S-palmitoylation is actively regulated by eraser enzymes that respond to alterations in mitochondrial lipid homeostasis.
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